DMDB_EUBBA
ID DMDB_EUBBA Reviewed; 163 AA.
AC Q0QLE1;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=2,3-dimethylmalate dehydratase small subunit {ECO:0000312|EMBL:ABC88409.1};
DE EC=4.2.1.85;
GN Name=DmdB {ECO:0000312|EMBL:ABC88409.1};
OS Eubacterium barkeri (Clostridium barkeri).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1528;
RN [1] {ECO:0000312|EMBL:ABC88409.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=ATCC 25849 / DSM 1223 / JCM 1389 / NCIMB 10623 / VKM B-1775 / VPI
RC 5359 {ECO:0000312|EMBL:ABC88409.1};
RX PubMed=16894175; DOI=10.1073/pnas.0601635103;
RA Alhapel A., Darley D.J., Wagener N., Eckel E., Elsner N., Pierik A.J.;
RT "Molecular and functional analysis of nicotinate catabolism in Eubacterium
RT barkeri.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12341-12346(2006).
RN [2] {ECO:0000305}
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC STRAIN=ATCC 25849 / DSM 1223 / JCM 1389 / NCIMB 10623 / VKM B-1775 / VPI
RC 5359 {ECO:0000269|PubMed:6489933};
RX PubMed=6489933; DOI=10.1515/bchm2.1984.365.2.847;
RA Kollmann-Koch A., Eggerer H.;
RT "Nicotinic acid metabolism. Dimethylmaleate hydratase.";
RL Hoppe-Seyler's Z. Physiol. Chem. 365:847-857(1984).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-2,3-dimethylmalate = dimethylmaleate + H2O;
CC Xref=Rhea:RHEA:20253, ChEBI:CHEBI:15377, ChEBI:CHEBI:17081,
CC ChEBI:CHEBI:57422; EC=4.2.1.85;
CC Evidence={ECO:0000269|PubMed:6489933};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.1 mM for dimethylmaleate {ECO:0000269|PubMed:6489933};
CC pH dependence:
CC Highly active between pH 6.5 and 9.0. Retains 50% and 10% of maximum
CC activity at pH 5.0 and 4.5 respectively.
CC {ECO:0000269|PubMed:6489933};
CC -!- PATHWAY: Cofactor degradation; nicotinate degradation; propanoate and
CC pyruvate from 6-hydroxynicotinate: step 7/8.
CC {ECO:0000269|PubMed:16894175}.
CC -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC {ECO:0000250|UniProtKB:A6LPX5}.
CC -!- INDUCTION: By nicotinic acid. {ECO:0000269|PubMed:6489933}.
CC -!- SIMILARITY: Belongs to the LeuD family. LeuD type 2 subfamily.
CC {ECO:0000305}.
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DR EMBL; DQ310789; ABC88409.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0QLE1; -.
DR SMR; Q0QLE1; -.
DR STRING; 1528.SAMN04488579_1123; -.
DR KEGG; ag:ABC88409; -.
DR BioCyc; MetaCyc:MON-13677; -.
DR UniPathway; UPA01010; UER01018.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047868; F:dimethylmaleate hydratase activity; IDA:UniProtKB.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:1901848; P:nicotinate catabolic process; IDA:GO_Central.
DR CDD; cd01577; IPMI_Swivel; 1.
DR Gene3D; 3.20.19.10; -; 1.
DR HAMAP; MF_01032; LeuD_type2; 1.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR033940; IPMI_Swivel.
DR InterPro; IPR011824; LeuD/DmdB_bac.
DR InterPro; IPR011827; LeuD_type2/HacB/DmdB.
DR Pfam; PF00694; Aconitase_C; 1.
DR TIGRFAMs; TIGR02084; leud; 1.
DR TIGRFAMs; TIGR02087; LEUD_arch; 1.
PE 1: Evidence at protein level;
KW Lyase.
FT CHAIN 1..163
FT /note="2,3-dimethylmalate dehydratase small subunit"
FT /id="PRO_0000403995"
SQ SEQUENCE 163 AA; 17369 MW; 6A2E9CBA57AEF3EE CRC64;
MKAKGSVFRY GDNVDTDVII PARFLNTSDP LELAAHCMED IDADFSSKVN AGDIIVADDN
FGCGSSREHA PISIKASGVS CVIANSFARI FYRNAINIGL PILECPEAVA VIEAGDEVEV
DFDSGVITDV TKGQSFQGQA FPEFMQTLIA AGGLVNYINA TEK
